The mechanism of 3-hydroxy epimerization of chenodeoxycholic acid by Clostridium perfringens was investigated in 3 alpha, 7 α-dihydroxy-[2,2,4,4-2H4]-, 3 alpha, 7 α-dihydroxy-[3 β-2H]- and 3 beta, 7 α-dihydroxy-[3 α-2H]-5 β-cholanoic acid transformations. Our findings rule out a dehydration-rehydration pathway and agree with a redox mechanism involving 3-oxochenodeoxycholic acid as intermediate.

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